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Chlorine in PDB 5nl1: Shigella Ipaa-VBS3/Tbs in Complex with the Talin VBS1 Domain 488-512

Protein crystallography data

The structure of Shigella Ipaa-VBS3/Tbs in Complex with the Talin VBS1 Domain 488-512, PDB code: 5nl1 was solved by C.Bou-Nader, L.Pecqueur, C.Valencia-Gallardo, M.Fontecave, G.Tran Vannhieu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.33 / 2.50
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 66.260, 96.360, 175.690, 90.00, 90.00, 90.00
R / Rfree (%) 19.6 / 22.8

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Shigella Ipaa-VBS3/Tbs in Complex with the Talin VBS1 Domain 488-512 (pdb code 5nl1). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Shigella Ipaa-VBS3/Tbs in Complex with the Talin VBS1 Domain 488-512, PDB code: 5nl1:

Chlorine binding site 1 out of 1 in 5nl1

Go back to Chlorine Binding Sites List in 5nl1
Chlorine binding site 1 out of 1 in the Shigella Ipaa-VBS3/Tbs in Complex with the Talin VBS1 Domain 488-512


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Shigella Ipaa-VBS3/Tbs in Complex with the Talin VBS1 Domain 488-512 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cl701

b:91.7
occ:1.00
OG1 D:THR571 3.1 76.2 1.0
N D:THR571 3.7 62.0 1.0
N D:TYR570 3.8 64.1 1.0
CB D:THR571 3.9 71.4 1.0
OD1 D:ASP569 4.0 73.5 1.0
CB D:TYR570 4.4 65.6 1.0
CA D:TYR570 4.4 62.5 1.0
CA D:THR571 4.4 61.1 1.0
C D:ASP569 4.4 68.0 1.0
C D:TYR570 4.5 64.6 1.0
CA D:ASP569 4.6 68.2 1.0
O D:THR568 5.0 79.2 1.0
CG D:ASP569 5.0 73.6 1.0

Reference:

C.Valencia-Gallardo, C.Bou-Nader, D.I.Aguilar-Salvador, N.Carayol, N.Quenech'du, L.Pecqueur, H.Park, M.Fontecave, T.Izard, G.Tran Van Nhieu. Shigella Ipaa Binding to Talin Stimulates Filopodial Capture and Cell Adhesion. Cell Rep V. 26 921 2019.
ISSN: ESSN 2211-1247
PubMed: 30673614
DOI: 10.1016/J.CELREP.2018.12.091
Page generated: Sat Dec 12 12:10:01 2020

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